The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions.
Open Access
- 1 March 1989
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 108 (3) , 779-787
- https://doi.org/10.1083/jcb.108.3.779
Abstract
The major product of the XLR (X-chromosomal, lymphocyte-regulated) locus is found to be a 30-kD nuclear protein with a relatively short (t1/2 approximately equal to 2 h) half-life. Together with its stage- and tissue-specific pattern of expression, this suggests a role for this protein in the regulation of differentiation in T and B lymphocytes. Interestingly, the XLR protein almost completely leaches out of the nucleus after lysis of cells in low salt buffer, but is stabilized in that location by metal cations, particularly Zn++. This stabilization is reversible by chelating agents (o-phenanthroline, EDTA) which also release a number of other polypeptides in addition to XLR. These results suggest that XLR represents a novel class of nuclear proteins, and that cations such as zinc may play a role in the localization of these proteins in the nucleus.This publication has 34 references indexed in Scilit:
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